| 3-chloro-D-alanine dehydrochlorinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.5.1.2 | ||||||||
| CAS no. | 78990-65-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
- 3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 (overall reaction)
- (1a) 3-chloro-D-alanine = chloride + 2-aminoprop-2-enoate
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming). Other names in common use include β-chloro-D-alanine dehydrochlorinase, and 3-chloro-D-alanine chloride-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
- Nagasawa T, Ishii T, Yamada H (1988). "Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1". Archives of Microbiology. 149 (5): 413–6. doi: 10.1007/BF00425580. PMID 3132906.
- Yamada H, Nagasawa T, Ohkishi H, Kawakami B, Tani Y (June 1981). "Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida". Biochemical and Biophysical Research Communications. 100 (3): 1104–10. doi: 10.1016/0006-291X(81)91937-9. PMID 6791643.
| 3-chloro-D-alanine dehydrochlorinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.5.1.2 | ||||||||
| CAS no. | 78990-65-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
- 3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 (overall reaction)
- (1a) 3-chloro-D-alanine = chloride + 2-aminoprop-2-enoate
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming). Other names in common use include β-chloro-D-alanine dehydrochlorinase, and 3-chloro-D-alanine chloride-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
- Nagasawa T, Ishii T, Yamada H (1988). "Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1". Archives of Microbiology. 149 (5): 413–6. doi: 10.1007/BF00425580. PMID 3132906.
- Yamada H, Nagasawa T, Ohkishi H, Kawakami B, Tani Y (June 1981). "Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida". Biochemical and Biophysical Research Communications. 100 (3): 1104–10. doi: 10.1016/0006-291X(81)91937-9. PMID 6791643.